Digital Commons Network^™

Exploring Indicator Displacement Assays For Phosphate Detection In Seawater, Francis Radics

Chemistry & Biochemistry Student Scholarship

Francis Radics ’22
Major: Biochemistry
Faculty Mentor: Dr. John Breen, Chemistry and Biochemistry

Indicator displacement assays are based on the optical signal modulation of a noncovalently bound indicator upon dissociation by an analyte species. Our work has focused on exploring the lower detection limits for luminescent displacement assays for inorganic phosphate in seawater using complex ions containing two di(2-picolyl)amine ligands (also called DPA or bis(2-pyridylmethyl)amine), each coordinating a zinc cation. Following the work of B.D. Smith and coworkers, we have prepared three ligands by covalently attaching two DPA moieties, 2,6-bis(chloromethyl) benzene, and 2,6-bis(chloromethyl)-4-methylphenol, and 1,2-phenylenedimethylamine, for assays with 6,7-dihydroxy-4-methanesulfonic acid …

The Discovery And Analysis Of Mycobacteriophage “Rita”, Anna Fakhri

Chemistry & Biochemistry Student Scholarship

Anna Fakhri ’24
Major: Biochemistry
Faculty Mentor: Dr. Kathleen Cornely, Chemistry and Biochemistry

Mycobacteriophage “Rita” was isolated on Mycobacterium smegmatis mc2155 from an enriched soil sample from North Easton, Massachusetts. As Rita infects Mycobacterium smegmatis, further study of the phage was completed in order to determine its ability to be utilized in phage therapy for infections caused by pathogenic Mycobacterium, such as Mycobacterium tuberculosis and Mycobacterium abscessus. Once isolated, the phage DNA was analyzed through PCR to determine the phage belonged to cluster F and subcluster F1. The phage DNA was sequenced, and a genome annotation was completed. The annotation …

Characterization Of Immunity Systems In A Cluster Phages, Katherine Cleary

Chemistry & Biochemistry Student Scholarship

Katherine Cleary ’23
Major: Biochemistry
Faculty Mentor: Dr. Kathleen A. Cornely, Chemistry and Biochemistry

Bacteriophages are viruses that infect bacteria. Bacteriophages may use two different cycles to infect their hosts, which are the lytic cycle and the lysogenic cycle. During the lysogenic cycle, the phage genome integrates into the bacteria chromosome and becomes a part of the host. If a phage remains in the lysogenic cycle, the host is susceptible to infection from other bacteriophages. This process is known as superinfection and it can have a variety of outcomes. Homoimmunity occurs when the phages have similar repressor proteins. Heteroimmunity occurs …

Development And Kinetic Survey Of A G148t Mutant Human Cytosolic Malate Dehydrogenase Isoform 3 Enzyme With Oxaloacetate And A-Ketoglutarate, Ethan N. Dionne

Chemistry & Biochemistry Student Scholarship

Cancer cells often use an altered metabolic pathway in which glycolysis, uncoupled from the citric acid cycle, serves as the primary source of ATP. To support cancer cell proliferation and growth, the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) must have a constant source of NAD. While lactate dehydrogenase (LDH) in its conversion of pyruvate to lactate is a well-known source of cytosolic NAD for GAPDH activity, cytosolic malate dehydrogenase (MDH1) also plays a role in cell proliferation through its generation of cytosolic NAD by the conversion of OAA to malate. This development has implicated MDH1 in cancer cell metabolism and characterizing …

Proline To Serine Mutation In The Active Site Loop Of Malate Dehydrogenase Alters Substrate Specificity, Olivia J. Schmitt

Chemistry & Biochemistry Student Scholarship

Cancer cells preferentially undergo glycolysis in aerobic environments, a phenomenon termed the Warburg effect. Malate dehydrogenase (MDH) catalyzes the reversible interconversion of malate and oxaloacetate. Human cytosolic malate dehydrogenase (hMDH1) isoform 3 is involved in the malate-aspartate shuttle (MAS), which oxidizes cytosolic NADH. hMDH1 is implicated in high aerobic glycolysis in cancer cells because NAD is a necessary cofactor for glycolysis. Thus, hMDH1 is a promising molecular target for cancer treatment. A single proline residue at position 110 in the mobile active site loop of hMDH1 was mutated to a serine with the intention of altering the enzyme’s substrate specificity. …